Fibroin membrane was used as a support for immobilized β-glucosidase. The immobilized enzyme was prepared by drying fibroin-enzyme solution on a horizontal plate, followed by ethyl alcohol treatment which was an essential process for immobilization. The immobilized β-glucosidase was characterized enzymatically compared with soluble enzyme, using p-nitrophenyl-β-D-glucopyranoside as a substrate. The immobilized enzyme showed 47% of the activity of soluble enzyme and little decrease of the activity was observed both on re-use and storage. There were no significant differences in pH dependency between immobilized and soluble enzyme activity. Activation energy was slightly larger with immobilized enzyme than soluble enzyme. The enzyme was considerably enhanced by immobilization in stabilities against heating, electrodialysis and protease treatment. Apparent affinity for the substrate decreased as membrane thickness increased. Enzyme affinity for substrate in the membrane was discussed.
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Miyairi et al. (1978) studied this question.